BBKI_BAUBA
ID BBKI_BAUBA Reviewed; 164 AA.
AC P83052;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Kunitz-type serine protease inhibitor BbKI;
OS Bauhinia bauhinioides (Perlebia bauhinoides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Cercidoideae; Cercideae; Bauhiniinae;
OC Bauhinia.
OX NCBI_TaxID=166014 {ECO:0000305};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, AND SUBUNIT.
RC TISSUE=Seed;
RX PubMed=11375765; DOI=10.2174/0929867013372779;
RA Oliva M.L.V., Mendes C.R., Santomauro-Vaz E.M., Juliano M.A., Mentele R.,
RA Auerswald E.A., Sampaio M.U., Sampaio C.A.M.;
RT "Bauhinia bauhinioides plasma kallikrein inhibitor: interaction with
RT synthetic peptides and fluorogenic peptide substrates related to the
RT reactive site sequence.";
RL Curr. Med. Chem. 8:977-984(2001).
CC -!- FUNCTION: Inhibits bovine trypsin, human plasma kallikrein and plasmin
CC and weakly bovine chymotrypsin. {ECO:0000269|PubMed:11375765}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermolabile.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11375765}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC type inhibitor) family. {ECO:0000305}.
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DR PDB; 4ZOT; X-ray; 1.40 A; A=1-164.
DR PDB; 7JOD; X-ray; 1.33 A; I=1-164.
DR PDB; 7JOE; X-ray; 2.60 A; I=1-164.
DR PDB; 7JOS; X-ray; 2.10 A; B/D/F/H/J/L/N=1-164.
DR PDB; 7JOW; X-ray; 1.91 A; I=1-162.
DR PDB; 7JQK; X-ray; 1.33 A; I=1-164.
DR PDB; 7JQN; X-ray; 1.50 A; I=1-164.
DR PDB; 7JQO; X-ray; 1.60 A; I=1-164.
DR PDB; 7JQV; X-ray; 2.10 A; I=1-164.
DR PDB; 7JR1; X-ray; 2.05 A; G/H/I/J/K/L=1-162.
DR PDB; 7JR2; X-ray; 1.85 A; G/H/I/J/K/L=1-162.
DR PDB; 7JRX; X-ray; 1.77 A; I/i=1-164.
DR PDBsum; 4ZOT; -.
DR PDBsum; 7JOD; -.
DR PDBsum; 7JOE; -.
DR PDBsum; 7JOS; -.
DR PDBsum; 7JOW; -.
DR PDBsum; 7JQK; -.
DR PDBsum; 7JQN; -.
DR PDBsum; 7JQO; -.
DR PDBsum; 7JQV; -.
DR PDBsum; 7JR1; -.
DR PDBsum; 7JR2; -.
DR PDBsum; 7JRX; -.
DR AlphaFoldDB; P83052; -.
DR SMR; P83052; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
DR InterPro; IPR002160; Prot_inh_Kunz-lg.
DR PANTHER; PTHR33107; PTHR33107; 1.
DR Pfam; PF00197; Kunitz_legume; 1.
DR SMART; SM00452; STI; 1.
DR SUPFAM; SSF50386; SSF50386; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Protease inhibitor; Secreted;
KW Serine protease inhibitor.
FT CHAIN 1..164
FT /note="Kunitz-type serine protease inhibitor BbKI"
FT /id="PRO_0000083295"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:4ZOT"
FT STRAND 18..27
FT /evidence="ECO:0007829|PDB:4ZOT"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:4ZOT"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:4ZOT"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:4ZOT"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:4ZOT"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:4ZOT"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:4ZOT"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:4ZOT"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:4ZOT"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:4ZOT"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:4ZOT"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:4ZOT"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:4ZOT"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:4ZOT"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:4ZOT"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:4ZOT"
SQ SEQUENCE 164 AA; 17972 MW; 0EB469D4611DD030 CRC64;
SVVVDTNGQP VSNGADAYYL VPVSHGHAGL ALAKIGNEAE PRAVVLDPHH RPGLPVRFES
PLRINIIKES YFLNIKFGPS SSDSGVWDVI QQDPIGLAVK VTDTKSLLGP FKVEKEGEGY
KIVYYPERGQ TGLDIGLVHR NDKYYLAVKD GEPCVFKIRK ATDE